| + |
PRKCA | up-regulates 
phosphorylation
|
PLEK |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28880 |
Ser113 |
GQKFARKsTRRSIRL |
Homo sapiens |
|
| pmid |
sentence |
| 7559487 |
Pleckstrin is a substrate for protein kinase c / a combination of phosphopeptide analysis and site-directed mutagenesis shows that three residues in the intervening sequence between the two pleckstrin ph domains become phosphorylated: ser113, thr114, and ser117. /these results suggest that the phosphorylation of at least two of the sites is required for maximal pleckstrin activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40048 |
Ser117 |
ARKSTRRsIRLPETI |
Homo sapiens |
|
| pmid |
sentence |
| 8615792 |
To determine the role of pkc-dependent phosphorylation in pleckstrin function, we mapped the phosphorylation sites in vivo of wild-type and site-directed mutants of pleckstrin expressed in cos cells. Phosphorylation was found to occur almost exclusively on ser-113 and ser-117. Replacing all these sites with glycine decreased phosphorylation by > 90% and reduced pleckstrin's ability to inhibit phosphoinositide hydrolysis by as much as 80%. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28884 |
Ser117 |
ARKSTRRsIRLPETI |
Homo sapiens |
|
| pmid |
sentence |
| 7559487 |
To determine the role of pkc-dependent phosphorylation in pleckstrin function, we mapped the phosphorylation sites in vivo of wild-type and site-directed mutants of pleckstrin expressed in cos cells. Phosphorylation was found to occur almost exclusively on ser-113 and ser-117. Replacing all these sites with glycine decreased phosphorylation by > 90% and reduced pleckstrin's ability to inhibit phosphoinositide hydrolysis by as much as 80%. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
PLEK
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3.0